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The Nobel Prize in Chemistry
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The first protein crystal structures were reported by Max Perutz and Sir John Kendrew in 1960, and these two investigators shared the Nobel Prize for Chemistry in 1962. Perutz had started studying the oxygen-carrying blood pigment, hemoglobin, with Sir Lawrence Bragg in Cambridge already in 1937, and ten years later he was joined by Kendrew, who looked at crystals of the related muscle pigment, myoglobin. These proteins are both rich in Pauling's -helix (see Section 3.4), and this made it possible to discern the main features of the structures at the relatively low resolution first used. The same year that Perutz and Kendrew won their prize, the Nobel Prize for Physiology or Medicine went to Francis Crick, James Watson and Maurice Wilkins "for their discoveries concerning the molecular structure of nucleic acids ... ." Two years later (1964) Dorothy Crowfoot Hodgkin received the Nobel Prize for Chemistry for determining the crystal structures of penicillin and vitamin B12.
Two later Nobel Prizes for Chemistry in the crystallographic field were given for work on structures of relatively small molecules. William N. Lipscomb of Harvard received the prize in 1976 "for his studies on the structures of boranes illuminating problems of chemical bonding". In 1985 Herbert A. Hauptman of Buffalo and Jerome Karle of Washington, DC, shared the prize for "the development of direct methods for the determination of crystal structures". Their methods are called direct, because they yield the structure directly from the diffraction data collected, and they have been indispensable in the determination of the structures of a large number of natural products.
Crystallographic electron microscopy was developed by Sir Aaron Klug in Cambridge, who was awarded the Nobel Prize for Chemistry in 1982. With this technique Klug has investigated the structure of large nucleic acid-protein complexes, such as viruses and chromatin, the carrier of the genes in the cell nucleus. Many of the most important life processes are carried out by proteins associated with biological membranes. This is, for example, true of the two key processes in energy metabolism, respiration and photosynthesis. Attempts to prepare crystals of membrane proteins for structural studies were, however, for many years unsuccessful, but in 1982 Hartmut Michel, then at the Max-Planck-Institut in Martinsried, managed to crystallize a photosynthetic reaction center after a painstaking series of experiments.
He then proceeded to determine the three-dimensional structure of this protein complex in collaboration with Johann Deisenhofer and Robert Huber, and this was published in 1985. Deisenhofer, Huber and Michel shared the Nobel Prize for Chemistry in 1988. Michel has later also crystallized and determined the structure of the terminal enzyme in respiration, and his two structures have allowed detailed studies of electron transfer (cf. Sections 3.3 and 3.4) and its coupling to proton pumping, key features of the chemiosmotic mechanism for which Peter Mitchell had already received the Nobel Prize for Chemistry in 1978 (see Section 3.12). Functional and structural studies on the enzyme ATP synthase, connected to this proton pumping mechanism, was awarded one-half of the Nobel Prize for Chemistry in 1997, shared between Paul D. Boyer and John Walker (see Section 3.12).
3.6 Inorganic and Nuclear Chemistry
Much of the progress in inorganic chemistry during the 20th century has been associated with investigations of coordination compounds, i.e., a central metal ion surrounded by a number of coordinating groups, called ligands. In 1893 Alfred Werner in Zürich presented his coordination theory, and in 1905 he summarized his investigations in this new field in a book (Neuere Anschauungen auf dem Gebiete der anorganischen Chemie), which appeared in no less than five editions from 1905-1923. Compounds in which a metal ion binds several other molecules (ligands), for example, ammonia, had earlier been thought to have a linear structure, in accord with a theory advanced by the Swedish chemist Wilhelm Blomstrand in Lund. Werner showed that such a structure is inconsistent with some experimental facts, and he suggested instead that all the ligand molecules are bound directly to the metal ion. Werner was awarded the Nobel Prize for Chemistry in 1913. Taube's investigations of electron transfer, awarded in 1983 (see Section 3.3), were mainly carried out with coordination compounds, and vitamin B12 as well as the proteins hemoglobin and myoglobin, investigated by the Laureates Hodgkin, Perutz and Kendrew (see Section 3.5), also belong to this category.
Another early prize for work in inorganic chemistry was that to Fritz Haber from Berlin in 1918 "for the synthesis of ammonia from its elements", i.e., from nitrogen and hydrogen. The importance of this synthesis is above all in its industrial application in the form of the Haber-Bosch method, which had been developed by Carl Bosch as an improvement (cf. Nobel's will) of Haber's original procedure. It allows the manufacture of ammonia on a large scale, and the ammonia can then be used for the production of many different nitrogen-containing chemicals. Bosch shared the Nobel Prize for Chemistry with Friedrich Bergius in 1931 (see Section 3.13).
Much inorganic chemistry in the early 1900s was a consequence of the discovery of radioactivity in 1896, for which Henri Becquerel from Paris was awarded the Nobel Prize for Physics in 1903, together with Pierre and Marie Curie. In 1911 Marie Curie received the Nobel Prize for Chemistry for her discovery of the elements radium and polonium and for the isolation of radium and studies of its compounds, and this made her the first investigator to be awarded two Nobel Prizes. The prize in 1921 went to Frederick Soddy of Oxford for his work on the chemistry of radioactive substances and on the origin of isotopes. In 1934 Frédéric Joliot and his wife Irène Joliot-Curie, the daughter of the Curies, discovered artificial radioactivity, i.e., new radioactive elements produced by the bombardment of non-radioactive elements with -particles or neutrons. They were awarded the Nobel Prize for Chemistry in 1935 for "their synthesis of new radioactive elements".
Zdroje: Westgren, A., Nobel – The Man and His Prizes, ed. Odelberg, W. (Elsevier, New York, 1972), pp. 279-385., Kormos Barkan, D., Walther Nernst and the Transition in Modern Physical Science, (Cambridge University Press, 1999)., Rife, P., Lise Meitner and the Dawn of the Nuclear Age, (Birkhäuser, 1999).